Optimized and Robust Workflow for Quantifying the Canonical Histone Ubiquitination Marks H2AK119ub and H2BK120ub by LC–MS/MS

The eukaryotic genome is packaged around histone proteins, which are subject to a myriad of post-translational modifications. By controlling DNA accessibility and the recruitment of protein complexes that mediate chromatin-related processes, these modifications constitute a key mechanism of epigenet...

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Published inJournal of proteome research Vol. 23; no. 12; pp. 5405 - 5420
Main Authors Lopes, Mariana, Lund, Peder J., Garcia, Benjamin A.
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 06.12.2024
Subjects
Anhydrides
Chromatography, Liquid - methods
derivatization
digestion
DNA
epigenetics
genome
Histone Code
histones
Histones - metabolism
Humans
Liquid Chromatography-Mass Spectrometry
mass spectrometry
Propionates
Protein Processing, Post-Translational
proteome
Proteomics - methods
synthetic peptides
Tandem Mass Spectrometry - methods
ubiquitin
Ubiquitination
Workflow
histones
post-translational modifications
ubiquitination
epigenetics
LC−MS/MS
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Abstract The eukaryotic genome is packaged around histone proteins, which are subject to a myriad of post-translational modifications. By controlling DNA accessibility and the recruitment of protein complexes that mediate chromatin-related processes, these modifications constitute a key mechanism of epigenetic regulation. Since mass spectrometry can easily distinguish between these different modifications, it has become an essential technique in deciphering the histone code. Although robust LC–MS/MS methods are available to analyze modifications on the histone N-terminal tails, routine methods for characterizing ubiquitin marks on histone C-terminal regions, especially H2AK119ub, are less robust. Here, we report the development of a simple workflow for the detection and improved quantification of the canonical histone ubiquitination marks H2AK119ub and H2BK120ub. The method entails a fully tryptic digestion of acid-extracted histones, followed by derivatization with heavy or light propionic anhydride. A pooled sample is then spiked into oppositely labeled single samples as a reference channel for relative quantification, and data is acquired using PRM-based nano-LC–MS/MS. We validated our approach with synthetic peptides as well as treatments known to modulate the levels of H2AK119ub and H2BK120ub. This new method complements existing histone workflows, largely focused on the lysine-rich N-terminal regions, by extending modification analysis to other sequence contexts.
AbstractList The eukaryotic genome is packaged around histone proteins, which are subject to a myriad of post-translational modifications. By controlling DNA accessibility and the recruitment of protein complexes that mediate chromatin-related processes, these modifications constitute a key mechanism of epigenetic regulation. Since mass spectrometry can easily distinguish between these different modifications, it has become an essential technique in deciphering the histone code. Although robust LC-MS/MS methods are available to analyze modifications on the histone N-terminal tails, routine methods for characterizing ubiquitin marks on histone C-terminal regions, especially H2AK119ub, are less robust. Here, we report the development of a simple workflow for the detection and improved quantification of the canonical histone ubiquitination marks H2AK119ub and H2BK120ub. The method entails a fully tryptic digestion of acid-extracted histones, followed by derivatization with heavy or light propionic anhydride. A pooled sample is then spiked into oppositely labeled single samples as a reference channel for relative quantification, and data is acquired using PRM-based nano-LC-MS/MS. We validated our approach with synthetic peptides as well as treatments known to modulate the levels of H2AK119ub and H2BK120ub. This new method complements existing histone workflows, largely focused on the lysine-rich N-terminal regions, by extending modification analysis to other sequence contexts.
The eukaryotic genome is packaged around histone proteins, which are subject to a myriad of post-translational modifications. By controlling DNA accessibility and the recruitment of protein complexes that mediate chromatin-related processes, these modifications constitute a key mechanism of epigenetic regulation. Since mass spectrometry can easily distinguish between these different modifications, it has become an essential technique in deciphering the histone code. Although robust LC-MS/MS methods are available to analyze modifications on the histone N-terminal tails, routine methods for characterizing ubiquitin marks on histone C-terminal regions, especially H2AK119ub, are less robust. Here we report the development of a simple workflow for the detection and improved quantification of the canonical histone ubiquitination marks H2AK119ub and H2BK120ub. The method entails a fully tryptic digestion of acid-extracted histones followed by derivatization with heavy or light propionic anhydride. A pooled sample is then spiked into oppositely labeled single samples as a reference channel for relative quantification, and data is acquired using PRM-based nanoLC-MS/MS. We validated our approach with synthetic peptides as well as treatments known to modulate the levels of H2AK119ub and H2BK120ub. This new method complements existing histone workflows, largely focused on the lysine-rich N-terminal regions, by extending modification analysis to other sequence contexts.
The eukaryotic genome is packaged around histone proteins, which are subject to a myriad of post-translational modifications. By controlling DNA accessibility and the recruitment of protein complexes that mediate chromatin-related processes, these modifications constitute a key mechanism of epigenetic regulation. Since mass spectrometry can easily distinguish between these different modifications, it has become an essential technique in deciphering the histone code. Although robust LC-MS/MS methods are available to analyze modifications on the histone N-terminal tails, routine methods for characterizing ubiquitin marks on histone C-terminal regions, especially H2AK119ub, are less robust. Here, we report the development of a simple workflow for the detection and improved quantification of the canonical histone ubiquitination marks H2AK119ub and H2BK120ub. The method entails a fully tryptic digestion of acid-extracted histones, followed by derivatization with heavy or light propionic anhydride. A pooled sample is then spiked into oppositely labeled single samples as a reference channel for relative quantification, and data is acquired using PRM-based nano-LC-MS/MS. We validated our approach with synthetic peptides as well as treatments known to modulate the levels of H2AK119ub and H2BK120ub. This new method complements existing histone workflows, largely focused on the lysine-rich N-terminal regions, by extending modification analysis to other sequence contexts.The eukaryotic genome is packaged around histone proteins, which are subject to a myriad of post-translational modifications. By controlling DNA accessibility and the recruitment of protein complexes that mediate chromatin-related processes, these modifications constitute a key mechanism of epigenetic regulation. Since mass spectrometry can easily distinguish between these different modifications, it has become an essential technique in deciphering the histone code. Although robust LC-MS/MS methods are available to analyze modifications on the histone N-terminal tails, routine methods for characterizing ubiquitin marks on histone C-terminal regions, especially H2AK119ub, are less robust. Here, we report the development of a simple workflow for the detection and improved quantification of the canonical histone ubiquitination marks H2AK119ub and H2BK120ub. The method entails a fully tryptic digestion of acid-extracted histones, followed by derivatization with heavy or light propionic anhydride. A pooled sample is then spiked into oppositely labeled single samples as a reference channel for relative quantification, and data is acquired using PRM-based nano-LC-MS/MS. We validated our approach with synthetic peptides as well as treatments known to modulate the levels of H2AK119ub and H2BK120ub. This new method complements existing histone workflows, largely focused on the lysine-rich N-terminal regions, by extending modification analysis to other sequence contexts.
Author Lopes, Mariana
Garcia, Benjamin A.
Lund, Peder J.
AuthorAffiliation Department of Biochemistry and Molecular Biophysics, School of Medicine
Penn Epigenetics Institute, Department of Biochemistry and Biophysics, Perelman School of Medicine
Washington University in St. Louis
University of Pennsylvania
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  name: Washington University in St. Louis
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– name: 1 Penn Epigenetics Institute, Dept. of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/39556659$$D View this record in MEDLINE/PubMed
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CitedBy_id crossref_primary_10_1016_j_tig_2025_01_003
Cites_doi 10.1002/pmic.201400483
10.1128/MCB.22.17.6070-6078.2002
10.1016/j.molcel.2017.01.009
10.1038/nature08966
10.1016/S1097-2765(02)00826-2
10.1016/j.molcel.2005.01.007
10.1038/47412
10.1128/MCB.00241-07
10.1016/j.molcel.2011.02.015
10.1128/MCB.25.2.637-651.2005
10.1101/gad.1110503
10.1038/s41588-021-00856-5
10.1016/j.molcel.2007.11.002
10.1021/pr900777e
10.1038/nmeth.1446
10.1038/embor.2009.108
10.1093/bfgp/ell022
10.1038/nbt.1654
10.1038/s41420-021-00406-2
10.1016/j.molcel.2007.01.035
10.1186/s13072-017-0172-y
10.1126/science.1221711
10.1083/jcb.200906005
10.1021/acs.analchem.5b00072
10.1101/gr.261016.120
10.1038/nature04733
10.7554/elife.37892
10.1038/nchembio.501
10.1016/j.cell.2013.03.008
10.1126/science.aac5681
10.1074/jbc.m112.361824
10.1038/ncomms13661
10.1038/nrm4067
10.1038/nprot.2010.192
10.1074/mcp.M600007-MCP200
10.1186/s13072-015-0006-8
10.1016/j.molcel.2013.01.034
10.1038/nature06906
10.1016/j.cell.2012.12.033
10.1126/science.1076997
10.1016/j.tibs.2020.11.005
10.1021/pr800468j
10.1016/j.cell.2009.02.027
10.1016/j.molcel.2012.01.002
10.1038/s41586-019-1038-1
10.1016/j.cell.2014.05.004
10.1126/science.1194472
10.1016/S0003-2697(03)00032-0
10.1021/acs.jproteome.8b00133
10.1016/j.molcel.2011.02.002
10.1126/science.abc3393
10.1016/j.molcel.2018.03.005
10.1016/j.ymeth.2020.01.013
10.1021/cr500373h
10.1016/j.celrep.2013.07.014
10.3791/54112
10.1038/s41467-019-10136-w
10.3389/fgene.2016.00122
10.1016/S1097-2765(02)00802-X
10.1074/jbc.M115.661553
10.1021/bi00429a006
10.1101/gad.1144003
10.1016/j.molcel.2019.11.021
10.1016/j.molcel.2011.01.024
10.1038/nrc3459
10.1101/gad.269603
10.1002/bies.201900192
10.1016/j.molcel.2016.03.030
10.1016/j.cell.2006.04.029
10.1006/bbrc.1994.2188
10.1158/0008-5472.CAN-11-2209
10.1016/j.celrep.2014.04.012
10.1093/nar/gkab1038
10.1016/j.ymeth.2019.12.001
10.1007/978-1-4939-9232-4_5
10.1016/j.molcel.2007.12.011
10.1007/978-1-4939-2999-3_24
10.1128/MCB.25.14.6123-6139.2005
10.1016/bs.ctdb.2019.11.002
10.1007/s00216-015-8725-z
10.1016/j.molcel.2014.04.013
10.1016/j.tig.2020.12.005
10.1016/j.molcel.2008.04.025
10.1016/S0076-6879(03)76015-7
10.1016/j.molcel.2004.05.009
10.1016/j.cell.2011.12.029
10.1038/nprot.2007.106
10.1016/bs.mie.2016.09.029
10.1038/ncb1712
10.1016/j.jmb.2024.168442
10.1038/nature02985
10.1038/nsmb.2833
10.1074/mcp.M114.046011
10.1101/gad.271841.115
10.1186/gb-2012-13-10-r85
10.1016/j.molcel.2019.10.013
10.1038/s41418-020-00709-4
10.1074/mcp.O114.046573
10.1158/2159-8290.CD-19-1220
10.1074/jbc.M112.375204
10.1016/j.molcel.2007.12.015
10.4161/cc.20919
10.1038/s41576-022-00468-7
10.1128/mcb.10.9.4905
10.1016/j.cell.2019.02.002
10.1038/nrg3607
10.1016/bs.mie.2015.12.007
10.1021/acs.analchem.5b03009
10.1074/mcp.tir118.001209
10.1038/nrg.2016.59
10.1128/mcb.00488-18
10.1021/pr9003739
10.1016/j.molcel.2012.09.019
10.1016/j.celrep.2019.01.058
10.1016/s0021-9258(19)40926-5
10.1074/jbc.C300494200
10.1002/pmic.201700309
10.1016/j.celrep.2014.07.025
10.1128/MCB.05231-11
10.1016/j.molcel.2011.05.015
10.1016/j.molcel.2011.08.025
10.1126/science.287.5452.501
10.1074/mcp.M500285-MCP200
10.1038/s41467-017-01384-9
10.1126/science.aat8950
10.1186/s13072-017-0139-z
10.1093/bioinformatics/btp033
10.1038/ng.912
10.1016/j.cell.2007.01.015
10.1002/mas.21406
10.1126/science.1232245
10.1074/jbc.M110.126813
10.1016/j.molcel.2008.02.014
10.1016/S0076-6879(05)02007-0
10.1016/1044-0305(95)00569-2
10.1007/s13361-019-02303-6
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Keywords histones
post-translational modifications
ubiquitination
epigenetics
LC−MS/MS
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PJL participated in project conception, performed experiments, analyzed data, and wrote the manuscript. ML performed experiments and assisted with drafting and revising the manuscript. BAG participated in project conception, provided oversight, assisted with manuscript revisions, and acquired funding.
Present Address: Dept. of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH 44106
CONTRIBUTIONS
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References ref45/cit45
ref99/cit99
ref3/cit3
ref81/cit81
ref16/cit16
ref52/cit52
ref114/cit114
ref23/cit23
ref115/cit115
ref116/cit116
ref110/cit110
ref111/cit111
ref2/cit2
ref112/cit112
ref77/cit77
ref113/cit113
ref71/cit71
ref117/cit117
ref20/cit20
ref48/cit48
ref118/cit118
ref74/cit74
ref119/cit119
ref10/cit10
ref35/cit35
ref89/cit89
ref19/cit19
ref93/cit93
ref42/cit42
ref96/cit96
ref107/cit107
ref120/cit120
ref109/cit109
ref13/cit13
ref122/cit122
ref105/cit105
ref61/cit61
ref67/cit67
ref38/cit38
ref128/cit128
ref90/cit90
ref124/cit124
ref64/cit64
ref126/cit126
ref54/cit54
ref6/cit6
ref18/cit18
ref136/cit136
ref65/cit65
ref97/cit97
ref101/cit101
ref11/cit11
ref102/cit102
ref29/cit29
ref76/cit76
ref86/cit86
ref32/cit32
ref39/cit39
ref5/cit5
ref43/cit43
ref80/cit80
ref133/cit133
ref28/cit28
ref132/cit132
ref91/cit91
ref55/cit55
ref12/cit12
ref66/cit66
ref22/cit22
ref121/cit121
ref33/cit33
ref87/cit87
ref106/cit106
ref129/cit129
ref44/cit44
ref70/cit70
ref98/cit98
ref125/cit125
ref9/cit9
ref27/cit27
ref63/cit63
ref56/cit56
ref92/cit92
ref8/cit8
ref31/cit31
ref59/cit59
ref85/cit85
ref34/cit34
ref37/cit37
ref60/cit60
ref88/cit88
ref17/cit17
ref82/cit82
ref53/cit53
ref21/cit21
ref46/cit46
ref49/cit49
ref75/cit75
ref24/cit24
ref50/cit50
ref78/cit78
ref36/cit36
ref83/cit83
ref79/cit79
ref100/cit100
ref25/cit25
ref103/cit103
ref72/cit72
ref14/cit14
ref57/cit57
ref51/cit51
ref134/cit134
ref135/cit135
ref40/cit40
ref68/cit68
ref94/cit94
ref130/cit130
ref131/cit131
ref26/cit26
ref73/cit73
ref69/cit69
ref15/cit15
ref62/cit62
ref41/cit41
ref58/cit58
ref95/cit95
ref108/cit108
ref104/cit104
ref4/cit4
ref30/cit30
ref47/cit47
ref84/cit84
ref127/cit127
ref1/cit1
ref123/cit123
ref7/cit7
38915586 - bioRxiv. 2024 Jun 13:2024.06.11.596744. doi: 10.1101/2024.06.11.596744.
References_xml – ident: ref91/cit91
  doi: 10.1002/pmic.201400483
– ident: ref20/cit20
  doi: 10.1128/MCB.22.17.6070-6078.2002
– ident: ref25/cit25
  doi: 10.1016/j.molcel.2017.01.009
– ident: ref39/cit39
  doi: 10.1038/nature08966
– ident: ref51/cit51
  doi: 10.1016/S1097-2765(02)00826-2
– ident: ref61/cit61
  doi: 10.1016/j.molcel.2005.01.007
– ident: ref3/cit3
  doi: 10.1038/47412
– ident: ref16/cit16
  doi: 10.1128/MCB.00241-07
– ident: ref83/cit83
  doi: 10.1016/j.molcel.2011.02.015
– ident: ref66/cit66
  doi: 10.1128/MCB.25.2.637-651.2005
– ident: ref33/cit33
  doi: 10.1101/gad.1110503
– ident: ref113/cit113
  doi: 10.1038/s41588-021-00856-5
– ident: ref18/cit18
  doi: 10.1016/j.molcel.2007.11.002
– ident: ref89/cit89
  doi: 10.1021/pr900777e
– ident: ref117/cit117
  doi: 10.1038/nmeth.1446
– ident: ref119/cit119
  doi: 10.1038/embor.2009.108
– ident: ref54/cit54
  doi: 10.1093/bfgp/ell022
– ident: ref108/cit108
  doi: 10.1038/nbt.1654
– ident: ref41/cit41
  doi: 10.1038/s41420-021-00406-2
– ident: ref81/cit81
  doi: 10.1016/j.molcel.2007.01.035
– ident: ref129/cit129
  doi: 10.1186/s13072-017-0172-y
– ident: ref40/cit40
  doi: 10.1126/science.1221711
– ident: ref79/cit79
  doi: 10.1083/jcb.200906005
– ident: ref123/cit123
  doi: 10.1021/acs.analchem.5b00072
– ident: ref112/cit112
  doi: 10.1101/gr.261016.120
– ident: ref36/cit36
  doi: 10.1038/nature04733
– ident: ref100/cit100
  doi: 10.7554/elife.37892
– ident: ref78/cit78
  doi: 10.1038/nchembio.501
– ident: ref10/cit10
  doi: 10.1016/j.cell.2013.03.008
– ident: ref58/cit58
  doi: 10.1126/science.aac5681
– ident: ref72/cit72
  doi: 10.1074/jbc.m112.361824
– ident: ref31/cit31
  doi: 10.1038/ncomms13661
– ident: ref23/cit23
  doi: 10.1038/nrm4067
– ident: ref118/cit118
  doi: 10.1038/nprot.2010.192
– ident: ref103/cit103
  doi: 10.1074/mcp.M600007-MCP200
– ident: ref111/cit111
  doi: 10.1186/s13072-015-0006-8
– ident: ref71/cit71
  doi: 10.1016/j.molcel.2013.01.034
– ident: ref73/cit73
  doi: 10.1038/nature06906
– ident: ref5/cit5
  doi: 10.1016/j.cell.2012.12.033
– ident: ref37/cit37
  doi: 10.1126/science.1076997
– ident: ref12/cit12
  doi: 10.1016/j.tibs.2020.11.005
– ident: ref105/cit105
  doi: 10.1021/pr800468j
– ident: ref69/cit69
  doi: 10.1016/j.cell.2009.02.027
– ident: ref22/cit22
  doi: 10.1016/j.molcel.2012.01.002
– ident: ref11/cit11
  doi: 10.1038/s41586-019-1038-1
– ident: ref28/cit28
  doi: 10.1016/j.cell.2014.05.004
– ident: ref47/cit47
  doi: 10.1126/science.1194472
– ident: ref99/cit99
  doi: 10.1016/S0003-2697(03)00032-0
– ident: ref116/cit116
  doi: 10.1021/acs.jproteome.8b00133
– ident: ref85/cit85
  doi: 10.1016/j.molcel.2011.02.002
– ident: ref26/cit26
  doi: 10.1126/science.abc3393
– ident: ref38/cit38
  doi: 10.1016/j.molcel.2018.03.005
– ident: ref125/cit125
  doi: 10.1016/j.ymeth.2020.01.013
– ident: ref1/cit1
  doi: 10.1021/cr500373h
– ident: ref77/cit77
  doi: 10.1016/j.celrep.2013.07.014
– ident: ref93/cit93
  doi: 10.3791/54112
– ident: ref102/cit102
  doi: 10.1038/s41467-019-10136-w
– ident: ref121/cit121
  doi: 10.3389/fgene.2016.00122
– ident: ref52/cit52
  doi: 10.1016/S1097-2765(02)00802-X
– ident: ref42/cit42
  doi: 10.1074/jbc.M115.661553
– ident: ref49/cit49
  doi: 10.1021/bi00429a006
– ident: ref57/cit57
  doi: 10.1101/gad.1144003
– ident: ref30/cit30
  doi: 10.1016/j.molcel.2019.11.021
– ident: ref53/cit53
  doi: 10.1016/j.molcel.2011.01.024
– ident: ref44/cit44
  doi: 10.1038/nrc3459
– ident: ref34/cit34
  doi: 10.1101/gad.269603
– ident: ref24/cit24
  doi: 10.1002/bies.201900192
– ident: ref63/cit63
  doi: 10.1016/j.molcel.2016.03.030
– ident: ref65/cit65
  doi: 10.1016/j.cell.2006.04.029
– ident: ref48/cit48
  doi: 10.1006/bbrc.1994.2188
– ident: ref87/cit87
  doi: 10.1158/0008-5472.CAN-11-2209
– ident: ref27/cit27
  doi: 10.1016/j.celrep.2014.04.012
– ident: ref114/cit114
  doi: 10.1093/nar/gkab1038
– ident: ref98/cit98
  doi: 10.1016/j.ymeth.2019.12.001
– ident: ref95/cit95
  doi: 10.1007/978-1-4939-9232-4_5
– ident: ref60/cit60
  doi: 10.1016/j.molcel.2007.12.011
– ident: ref133/cit133
  doi: 10.1007/978-1-4939-2999-3_24
– ident: ref62/cit62
  doi: 10.1128/MCB.25.14.6123-6139.2005
– ident: ref8/cit8
  doi: 10.1016/bs.ctdb.2019.11.002
– ident: ref130/cit130
  doi: 10.1007/s00216-015-8725-z
– ident: ref68/cit68
  doi: 10.1016/j.molcel.2014.04.013
– ident: ref120/cit120
  doi: 10.1016/j.tig.2020.12.005
– ident: ref80/cit80
  doi: 10.1016/j.molcel.2008.04.025
– ident: ref131/cit131
  doi: 10.1016/S0076-6879(03)76015-7
– ident: ref35/cit35
  doi: 10.1016/j.molcel.2004.05.009
– ident: ref32/cit32
  doi: 10.1016/j.cell.2011.12.029
– ident: ref88/cit88
  doi: 10.1038/nprot.2007.106
– ident: ref97/cit97
  doi: 10.1016/bs.mie.2016.09.029
– ident: ref64/cit64
  doi: 10.1038/ncb1712
– ident: ref76/cit76
  doi: 10.1016/j.jmb.2024.168442
– ident: ref21/cit21
  doi: 10.1038/nature02985
– ident: ref29/cit29
  doi: 10.1038/nsmb.2833
– ident: ref115/cit115
  doi: 10.1074/mcp.M114.046011
– ident: ref14/cit14
  doi: 10.1101/gad.271841.115
– ident: ref104/cit104
  doi: 10.1186/gb-2012-13-10-r85
– ident: ref70/cit70
  doi: 10.1016/j.molcel.2019.10.013
– ident: ref43/cit43
  doi: 10.1038/s41418-020-00709-4
– ident: ref90/cit90
  doi: 10.1074/mcp.O114.046573
– ident: ref45/cit45
  doi: 10.1158/2159-8290.CD-19-1220
– ident: ref96/cit96
  doi: 10.1074/jbc.M112.375204
– ident: ref55/cit55
  doi: 10.1016/j.molcel.2007.12.015
– ident: ref101/cit101
  doi: 10.4161/cc.20919
– ident: ref4/cit4
  doi: 10.1038/s41576-022-00468-7
– ident: ref19/cit19
  doi: 10.1128/mcb.10.9.4905
– ident: ref74/cit74
  doi: 10.1016/j.cell.2019.02.002
– ident: ref6/cit6
  doi: 10.1038/nrg3607
– ident: ref94/cit94
  doi: 10.1016/bs.mie.2015.12.007
– ident: ref92/cit92
  doi: 10.1021/acs.analchem.5b03009
– ident: ref136/cit136
  doi: 10.1074/mcp.tir118.001209
– ident: ref2/cit2
  doi: 10.1038/nrg.2016.59
– ident: ref84/cit84
  doi: 10.1128/mcb.00488-18
– ident: ref109/cit109
  doi: 10.1021/pr9003739
– ident: ref86/cit86
  doi: 10.1016/j.molcel.2012.09.019
– ident: ref75/cit75
  doi: 10.1016/j.celrep.2019.01.058
– ident: ref17/cit17
  doi: 10.1016/s0021-9258(19)40926-5
– ident: ref56/cit56
  doi: 10.1074/jbc.C300494200
– ident: ref132/cit132
  doi: 10.1002/pmic.201700309
– ident: ref15/cit15
  doi: 10.1016/j.celrep.2014.07.025
– ident: ref59/cit59
  doi: 10.1128/MCB.05231-11
– ident: ref13/cit13
  doi: 10.1016/j.molcel.2011.05.015
– ident: ref107/cit107
  doi: 10.1016/j.molcel.2011.08.025
– ident: ref50/cit50
  doi: 10.1126/science.287.5452.501
– ident: ref106/cit106
  doi: 10.1074/mcp.M500285-MCP200
– ident: ref134/cit134
  doi: 10.1038/s41467-017-01384-9
– ident: ref7/cit7
  doi: 10.1126/science.aat8950
– ident: ref122/cit122
  doi: 10.1186/s13072-017-0139-z
– ident: ref135/cit135
  doi: 10.1093/bioinformatics/btp033
– ident: ref46/cit46
  doi: 10.1038/ng.912
– ident: ref67/cit67
  doi: 10.1016/j.cell.2007.01.015
– ident: ref127/cit127
  doi: 10.1002/mas.21406
– ident: ref9/cit9
  doi: 10.1126/science.1232245
– ident: ref110/cit110
  doi: 10.1074/jbc.M110.126813
– ident: ref82/cit82
  doi: 10.1016/j.molcel.2008.02.014
– ident: ref126/cit126
  doi: 10.1016/S0076-6879(05)02007-0
– ident: ref128/cit128
  doi: 10.1016/1044-0305(95)00569-2
– ident: ref124/cit124
  doi: 10.1007/s13361-019-02303-6
– reference: 38915586 - bioRxiv. 2024 Jun 13:2024.06.11.596744. doi: 10.1101/2024.06.11.596744.
SSID ssj0015703
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Snippet The eukaryotic genome is packaged around histone proteins, which are subject to a myriad of post-translational modifications. By controlling DNA accessibility...
SourceID pubmedcentral
proquest
pubmed
crossref
acs
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 5405
SubjectTerms Anhydrides
Chromatography, Liquid - methods
derivatization
digestion
DNA
epigenetics
genome
Histone Code
histones
Histones - metabolism
Humans
Liquid Chromatography-Mass Spectrometry
mass spectrometry
Propionates
Protein Processing, Post-Translational
proteome
Proteomics - methods
synthetic peptides
Tandem Mass Spectrometry - methods
ubiquitin
Ubiquitination
Workflow
Title Optimized and Robust Workflow for Quantifying the Canonical Histone Ubiquitination Marks H2AK119ub and H2BK120ub by LC–MS/MS
URI http://dx.doi.org/10.1021/acs.jproteome.4c00519
https://www.ncbi.nlm.nih.gov/pubmed/39556659
https://www.proquest.com/docview/3130206961
https://www.proquest.com/docview/3154238957
https://pubmed.ncbi.nlm.nih.gov/PMC11932154
Volume 23
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